Spontaneous Generation of Infectious Prion Disease in Transgenic Mice
Juan-María Torres
, Joaquín Castilla, Belén Pintado, Alfonso Gutiérrez-Adan, Olivier Andréoletti, Patricia Aguilar-Calvo, Ana-Isabel Arroba, Beatriz Parra-Arrondo, Isidro Ferrer, Jorge Manzanares, and Juan-Carlos Espinosa
Author affiliations: Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria, Madrid, Spain (J.-M. Torres, J. Castilla, B. Pintado, A. Gutiérrez-Adán P. Aguilar-Calvo, A.-I. Arroba, B. Parra-Arrondo, J.-C. Espinosa); Basque Foundation for Science, Bilbao, Spain (J. Castilla); Ecole Nationale Vétérinaire de Toulouse, Toulouse, France (O. Andréoletti); Hospitalet de Llobregat, Barcelona, Spain (I. Ferrer); Universidad Miguel Hernandez, Sant Joan d´Alacant, Spain (J. Manzanares)
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Figure 4
Figure 4. . . Comparative Western blot analyses of brain prion protein resistant to proteinase K digestion (PrPres) from BoPrP-Tg110 mice infected with bovine spongiform encephalopathy (BSE)-C, 113L-BSE, BSE-L, and BSE-H prions. Mice infected with newly generated 113L-BSE prion at first (P1), second (P2), and third (P3) passages are compared with mice infected with BSE-C (P1) (lane 4); BSE-L (P1) (lane 5); and BSE-H (P1) (lane 6) prions. Each panel was identified by using the monoclonal antibody (mAb) listed at the bottom left. The same quantities of PrPres were loaded in all lanes. BoPrP, bovine prion protein; 113L, leucine substitution at codon 113. Values on the right are molecular masses in kilodaltons.
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